DAGK_STAAR
ID DAGK_STAAR Reviewed; 315 AA.
AC Q6GFF9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Diacylglycerol kinase;
DE Short=DAG kinase;
DE Short=DAGK;
DE EC=2.7.1.107 {ECO:0000269|PubMed:18611377};
GN Name=dagK; Synonyms=dgkB; OrderedLocusNames=SAR1989;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP FUNCTION AS A DIACYLGLYCEROL KINASE.
RX PubMed=17535816; DOI=10.1074/jbc.m703536200;
RA Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT "Identification of a soluble diacylglycerol kinase required for
RT lipoteichoic acid production in Bacillus subtilis.";
RL J. Biol. Chem. 282:21738-21745(2007).
RN [3] {ECO:0007744|PDB:2QV7, ECO:0007744|PDB:2QVL}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH ADP
RP AND MAGNESIUM, SUBUNIT, COFACTOR, MUTAGENESIS OF ASP-68; PRO-91; THR-94;
RP ASN-96; ASP-97; ASP-124; GLU-168; ASP-216; ASP-271 AND GLU-273, ACTIVE
RP SITE, AND REACTION MECHANISM.
RX PubMed=18611377; DOI=10.1016/j.str.2008.03.019;
RA Miller D.J., Jerga A., Rock C.O., White S.W.;
RT "Analysis of the Staphylococcus aureus DgkB structure reveals a common
RT catalytic mechanism for the soluble diacylglycerol kinases.";
RL Structure 16:1036-1046(2008).
CC -!- FUNCTION: Catalyzes the phosphorylation of diacylglycerol (DAG) into
CC phosphatidic acid. Is a key enzyme involved in the production of
CC lipoteichoic acid by reintroducing DAG formed from the breakdown of
CC membrane phospholipids into the phosphatidylglycerol biosynthetic
CC pathway. {ECO:0000269|PubMed:17535816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000269|PubMed:18611377};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18611377};
CC Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC structural role and is required for catalytic activity.
CC {ECO:0000269|PubMed:18611377};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18611377}.
CC -!- INTERACTION:
CC Q6GFF9; Q6GFF9: dagK; NbExp=2; IntAct=EBI-15714341, EBI-15714341;
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
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DR EMBL; BX571856; CAG40975.1; -; Genomic_DNA.
DR RefSeq; WP_001231458.1; NC_002952.2.
DR PDB; 2QV7; X-ray; 2.30 A; A=1-315.
DR PDB; 2QVL; X-ray; 2.40 A; A=1-315.
DR PDBsum; 2QV7; -.
DR PDBsum; 2QVL; -.
DR AlphaFoldDB; Q6GFF9; -.
DR SMR; Q6GFF9; -.
DR DIP; DIP-46022N; -.
DR KEGG; sar:SAR1989; -.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OMA; GFDSRVN; -.
DR OrthoDB; 869726at2; -.
DR BioCyc; MetaCyc:MON-20007; -.
DR BRENDA; 2.7.1.107; 3352.
DR EvolutionaryTrace; Q6GFF9; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..315
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000386495"
FT DOMAIN 1..132
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 10..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 67..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18611377"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 68
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 91
FT /note="P->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 94
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 96
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 97
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 124
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 168
FT /note="E->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 216
FT /note="D->A: 5-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 271
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT MUTAGEN 273
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18611377"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:2QV7"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2QV7"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 185..199
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2QV7"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2QV7"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 280..292
FT /evidence="ECO:0007829|PDB:2QV7"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:2QVL"
SQ SEQUENCE 315 AA; 34902 MW; 5EA85BFC769E1D0C CRC64;
MRKRARIIYN PTSGKEQFKR ELPDALIKLE KAGYETSAYA TEKIGDATLE AERAMHENYD
VLIAAGGDGT LNEVVNGIAE KPNRPKLGVI PMGTVNDFGR ALHIPNDIMG ALDVIIEGHS
TKVDIGKMNN RYFINLAAGG QLTQVSYETP SKLKSIVGPF AYYIKGFEML PQMKAVDLRI
EYDGNVFQGE ALLFFLGLTN SMAGFEKLVP DAKLDDGYFT LIIVEKSNLA ELGHIMTLAS
RGEHTKHPKV IYEKAKAINI SSFTDLQLNV DGEYGGKLPA NFLNLERHID VFAPNDIVNE
ELINNDHVDD NLIEE
